231
© Springer Nature Switzerland AG 2021
A. Gani, B. A. Ashwar (eds.), Food biopolymers: Structural, functional
and nutraceutical properties, https://doi.org/10.1007/978-3-030-27061-2_10
Bioactive Peptides Derived from Different
Sources
Sajid Maqsood, Sabika Jafar, Mehvesh Mushtaq, and Priti Mudgil
Introduction
Bioactive peptides are defined as fractions of proteins, which have a specific
sequence that has a positive physiological effect and may influence health (Kitts and
Weiler 2003). The structure of bioactive peptides consists of amino acids linked
together by covalent (or also known as peptide) bonds, and an overall lower molecular weight compared to proteins. Proteins are building blocks of life which play a
critical role in the metabolic functions of the human body. Bioactive peptides
derived from proteins may thus impact human health by displaying multifunctional
activities and can be classified as antioxidative, antimicrobial, antihypertensive, opioid, immunomodulatory, and anti-thrombotic (Sanchez and Vazquez 2017).
Once released from the parent protein, the activity of a bioactive peptide is
dependent on two important parameters (1) amino acid sequence, and (2) amino
acid composition. Generally, the bioactive peptides are 2–20 amino acids long, and
contains hydrophobic amino acids as well as lysine, arginine or proline groups
(Moller et al. 2008; Sanchez and Vazquez 2017). It is reported that bioactive peptides show resistance to gastrointestinal digestion (Kitts and Weiler 2003), which is
an important property that is validated to prove the efficacy of the bioactive peptide.
The sources of bioactive peptides can largely be classified on the basis of animal
origin (milk, meat and egg), plant origin (cereals, pulses, fruit and fruit seeds) and
S. Maqsood (*) · S. Jafar · P. Mudgil
Food Science Department, College of Food and Agriculture, United Arab Emirates
University, Al-Ain, 15551, United Arab Emirates
e-mail: sajid.m@uaeu.ac.ae
M. Mushtaq
Department of Food Science and Technology, University of Kashmir,
Srinagar, Jammu and Kashmir, India
© Springer Nature Switzerland AG 2021
A. Gani, B. A. Ashwar (eds.), Food biopolymers: Structural, functional
and nutraceutical properties, https://doi.org/10.1007/978-3-030-27061-2_10
Bioactive Peptides Derived from Different
Sources
Sajid Maqsood, Sabika Jafar, Mehvesh Mushtaq, and Priti Mudgil
Introduction
Bioactive peptides are defined as fractions of proteins, which have a specific
sequence that has a positive physiological effect and may influence health (Kitts and
Weiler 2003). The structure of bioactive peptides consists of amino acids linked
together by covalent (or also known as peptide) bonds, and an overall lower molecular weight compared to proteins. Proteins are building blocks of life which play a
critical role in the metabolic functions of the human body. Bioactive peptides
derived from proteins may thus impact human health by displaying multifunctional
activities and can be classified as antioxidative, antimicrobial, antihypertensive, opioid, immunomodulatory, and anti-thrombotic (Sanchez and Vazquez 2017).
Once released from the parent protein, the activity of a bioactive peptide is
dependent on two important parameters (1) amino acid sequence, and (2) amino
acid composition. Generally, the bioactive peptides are 2–20 amino acids long, and
contains hydrophobic amino acids as well as lysine, arginine or proline groups
(Moller et al. 2008; Sanchez and Vazquez 2017). It is reported that bioactive peptides show resistance to gastrointestinal digestion (Kitts and Weiler 2003), which is
an important property that is validated to prove the efficacy of the bioactive peptide.
The sources of bioactive peptides can largely be classified on the basis of animal
origin (milk, meat and egg), plant origin (cereals, pulses, fruit and fruit seeds) and
S. Maqsood (*) · S. Jafar · P. Mudgil
Food Science Department, College of Food and Agriculture, United Arab Emirates
University, Al-Ain, 15551, United Arab Emirates
e-mail: sajid.m@uaeu.ac.ae
M. Mushtaq
Department of Food Science and Technology, University of Kashmir,
Srinagar, Jammu and Kashmir, India